Preparation of Heat-induced Transparent Gels from Egg White by the Control of pH and Ionic Strength of the Medium

Egg white was dialyzed against distilled water or diluted with water, and the precipitates formed were removed by centrifugation. The supernatant gave a transparent gel after being heated at an acidic pH (2–4). At other regions of pH, except for the highly alkaline region, the gel or suspension was turbid upon heating. Insufficient centrifugation of the dialyzed egg white or the addition of NaCl to the supernatant after centrifugation resulted in a turbid gel on heating at even acidic pH. The removal of the slight precipitate formed at low ionic strength and the maintenance of low ionic strength during heating were both necessary for production of a transparent gel.     

Protein Components Precipitated from Egg White by Removal of Salt

A precipitate that formed in egg white at low ionic strength affected the transparency of heat-induced gels prepared at pH 2-4 and low ionic strength. The precipitate solubilized with SDS solution containing 2-mercaptoethanol and urea included major proteins of the egg white, as shown by SDS-polyacrylamide gel electrophoresis. The bands of ovalbumin, conalbumin and other protein were smaller when the precipitate was washed with water, but lysozyme and ovomacroglobulin probably remained in the precipitate fraction. It seemed that ovalbumin, conalbumin, and other proteins co-precipitated with these two kinds of proteins. Lysozyme added to the supernatant of egg white after dialysis, did not appear to produce turbidity upon heating at pH 2.5, but whole egg white was converted to a turbid gel upon being heated at this pH.     

Comparison of Transparent Gels with Turbid Gels Prepared from Egg White: Creep Analysis of Gels

Egg white from which the precipitate occurring during dialysis against water had been removed gave a transparent gel on heating at lower salt concentrations and pH 3.54. The addition of NaCl or a shift of pH from 3.54 to 4.50 brought about the turbid gels. Creep analyses of these transparent and turbid gels were done using a four-element mechanical model. The instantaneous elastic modulus, E₀, Newtonian modulus, ηn and retarded viscoelastic moduli, E₁ and η₁ increased with NaCl up to 125 mM and then decreased with increase in NaCl concentration at pH 3.54. At 125 mM NaCl and pH 3.54, a translucent gel was obtained. E₀ and η₁ decreased with the temperature of the gel, while E₁ and η₁did not change depending of temperature.     

Rheological Properties of Heat-Induced Ovalbumin Gels Prepared by Two-step and One-step Heating Methods

Ovalbumin gave a transparent solution, transparent gel, or opaque gel on heating at low ionic strength, but a turbid gel, or turbid suspension at high ionic strength (one-step heating). The ovalbumin solution, once heated at low ionic strength, gave a transparent gel with a second heating at high ionic strength (two-step heating). Textural parameters of hardness and adhesiveness, viscoelastic parameters from creep curves, breaking energy and water-holding capacity of these gels were measured. Transparent gels by the one- or two-step heating were firm and elastic and had high water-holding capacity. Turbid gels by one-step heating were soft and less elastic and had low water-holding capacity. The relationship between gel properties and structure was discussed.     

Texture and Microstructure of Heat-Formed Egg White Gels

Egg white gels were formed by heating liquid egg white at various pH, protein, and NaCl levels at different temperatures and times of heating. Hardness, cohesiveness, and springiness of gels were measured. Serum was expressed from gels and evaluated by polyacrylamide gel electrophoresis. Selected samples were prepared for scanning electron microscopy. Gel hardness rose with increasing temperature, time, pH, and protein level, and decreased with added salt. Cohesiveness and springiness increased with time and temperature of heating. Expressed serum decreased as pH, time, temperature, and protein level were increased. Gels at pH 5 and 6 had a coarse, aggregated structure. At pH 9 protein strands and globules were arranged in a uniform matrix. Salt prompted aggregation of gels.     

A new process for preparing transparent alkalised duck egg and its quality

When fresh duck (Anas plotyrhyncus) eggs (pH 8·0–8·5) are heated, their albumen develops a turbid gel. Through appropriate alkalisation (pH 11·5–12·8), the gel's transparency can be increased. The transparency of the heated duck egg-white is affected by pH value, heating temperature, heating rate and salt concentration. This research deals with the process for preparing the transparent alkalised duck egg and the change in its quality when stored. If fresh duck eggs are pickled in a solution of 42 g NaOH+50 g NaCl litre^?1 (25·3°C) for 8 days, removed, put in a water bath and heated at 70°C for 10 min they become transparent, their hardness and penetration increasing with storage. Total bacterial count and volatile basic nitrogen also increase with storage. The total bacterial count and the volatile basic nitrogen were 4·6 × 10⁶ cfu g^?1, 0·32 mg g^?1 when stored at a temperature of under 25°C for 4 weeks, respectively.     

How micro-phase separation alters the heating rate effects on globular protein gelation

This study was conducted to determine how the combination of heating rate and pH can be used to alter viscoelastic properties and microstructure of egg white protein and whey protein isolate gels. Protein solutions (1% to 7% w/v protein, pH 3.0 to 8.5) were heated using a range of heating rates (0.2 to 60 °C/min) to achieve a final temperature of 80 °C. The gelation process and viscoelastic properties of formed gels were evaluated using small strain rheology. Single phase or micro-phase separated solution conditions were determined by confocal laser scanning microscopy. In the single phase region, gels prepared by the faster heating rates had the lowest rigidity at 80 °C; however, a common G' was achieved after holding for 4 h at 80 °C . On the other hand, under micro-phase separation conditions, faster heating rates allowed phase separated particles to be frozen in the network prior to precipitation. Thus, gels produced by slower heating rates had lower rigidities than gels produced by faster heating rates. The effect of heating rate appears to depend on if the solution is under single phase or micro-phase separated conditions. PRACTICAL APPLICATION: The effect of heating rate and/or time on protein gel firmness can be explained based on protein charge. When proteins have a high net negative charge and form soluble aggregates, there is no heating rate effect and gels with equal firmness will be formed if given enough time. In contrast, when electrostatic repulsion is low, there is a competition between protein precipitation and gel formation; thus, a faster heating rate produces a firmer gel.     

Strength of Protein Gels Prepared with Microbial Transglutaminase as Related to Reaction Conditions

Influence of gelling reaction conditions on the strength of several protein gels prepared with microbial transglutaminase (TGase) was investigated. A method was developed to gel proteins and measure gel breaking strength in a micro well plate. Enzyme concentration range for maximum gel breaking strength varied from 10 to 40 units/g protein. Maxima gel breaking strengths were achieved at 50°C for SPI, caseinate and gelatin and 65°C for egg yolk and egg white proteins. Optimum pH resulting in strong gels was pH 9 for SPI, caseinate, and egg yolk, and pH 6 for gelatin and egg white. Adjusting pH was promoted in egg white the formation of ?-(γ-glutamyl)lysine crosslinks and increased its gel breaking strength.     

Heat-Induced Aggregation of Egg White Proteins as Studied by Vertical Flat-Sheet Polyacrylamide Gel Electrophoresis

Heat-induced aggregation of proteins in egg white was investigated by a vertical flat-sheet polyacrylamide gel electrophoretic method. The fractional and step-wise aggregation of egg white proteins was caused by heating. Even with a heating time of 120 min, ovalbumin and globulins Al and A2 failed to aggregate in egg white (pH 7 and 9) at 70°C, and ovotransferrin and ovomucoid also did not aggregate in egg white at 60°C (pH 9) and 76°C (pH 7 and 9), respectively. The ovoinhibitor was much more unstable than ovomucoid under heat-treatment, and the time dependency of heat-induced aggregation of flavoprotein was greater than those of the other proteins in egg white.     

Formation of two types of gels from bovine myosin

Myosin was isolated from bovine m. semimembranosus and gels were formed by heat treatment at different pH values and ionic strengths. The gels were subjected to rigidity measurements and their microstructure was studied by scanning electron microscopy. This article provides evidence that myosin can form two completely different gel structures in the pH range 5.5–6.0, depending on ionic strength. Fine stranded gel structures were formed at low ionic strength (0.25M KCl), whereas coarsely aggregated gel structures were formed at high ionic strength (0.6M KCl). The fine stranded structure had a higher rigidity than the coarsely aggregated structure. It was found that all fine strand myosin gels were formed from turbid solutions and the aggregate gels from clear solutions. When the pH was lowered to 4 in 0.6M KCl a strand-type gel structure formed spontaneously on dialysis, even without heat treatment. This structure did not change in character on heating. It was concluded that the conditions required for the formation of strand-type myosin gels were already present before the heat treatment and that the strands were made up of myosin filaments at certain pH and ionic strength combinations, which produced a turbid solution. The strand-type structures were considered specific with regard to myosin interactions which was not the case for the aggregated structures. Variation of the heating temperature in the range 55 to 65°C had no major effect on the type of structure formed.     

鸭蛋清蛋白凝胶质构特性影响因素研究

以冻干鸭蛋清蛋白粉为原料,以凝胶硬度和弹性为指标,在探究鸭蛋清蛋白凝胶形成条件的基础上,考察金属离子对凝胶质构特性的影响。结果表明,鸭蛋清蛋白凝胶形成的最佳条件为：蛋清蛋白质量分数12.0%、pH 8.0、80 ℃加热40 min。不同浓度钠离子和钙离子对凝胶弹性的提高均有显著作用,高浓度钾离子作用不显著,镁离子、锌离子和亚铁离子的浓度较大时反而有抑制作用。镁离子对凝胶硬度增加有显著作用,钾离子无显著影响,钠离子和钙离子为先促进后稳定的趋势,锌离子和亚铁离子对凝胶硬度增加有抑制作用。     

Heat-induced gelation of whey protein at high pH studied by combined UV spectroscopy and refractive index measurement after size exclusion chromatography and by in-situ dynamic light scattering

Summary The interactions between β-lactoglobulin and α-lactalbumin involved in gelation at 67.5 °C at high pH and low salt concentration were studied by size exclusion chromatography, followed by UV and refractive index measurements, and by in-situ dynamic light scattering. This was achieved by choosing whey protein samples with different proportions of the two proteins. The ratio of absorbance at 280 nm to the refractive index was used to demonstrate that α-lactalbumin was incorporated in aggregates and gels and drastically changed the properties of the gel, making them much more turbid than the transparent gels formed by β-lactoglobulin alone at the same pH and ionic strength. At a ratio of 1:2 for α-lactalbumin relative to β-lactoglobulin in the samples, the gel consisted of a 1:1 mixture of the two proteins. The aggregates present after 10 min of heating at 67.5 °C had molar mass of about 6.10⁶ g/mol and a radius of gyration of about 40 nm. After gel formation the field autocorrelation function could be described as a power law over many decades of lag time for all samples, demonstrating selfsimilarity of the gel structure. The only exception to this was for the gel with high content of α-lactalbumin which showed an oscillatory behaviour of the autocorrelation function. Significant amounts of glycosylated caseino-macro-peptide were observed in many of the samples at the position of β-lactoglobulin. However it did not affect gelation as it remains in solution.     

Effect of NaCl on thermal aggregation of egg white proteins from duck egg

Thermal aggregation of duck egg white solution (1 mg protein/ml, pH 7) was monitored in the presence of different NaCl concentrations (0–6%, w/w) across the temperature range of 20–90 °C. Duck egg white solution exhibited higher turbidity with coincidental increases in surface hydrophobicity and decreases in sulfhydryl group content as temperatures increased from 70 to 90 °C (p < 0.05). As NaCl concentration increased, the negative charge decreased, with coincidental increases in particle size of aggregate after heating to 90 °C. As visualised by confocal laser scanning microscopy, larger clusters of protein aggregates were observed with increasing NaCl concentrations. Major duck egg white protein with molecular mass of 45 kDa disappeared in the presence of 2–6% NaCl after heating above 80 °C, regardless of concentrations. Therefore, NaCl, especially at high concentrations, could induce thermal aggregation of duck egg white protein, which could determine the characteristics of salted egg white after heating.     

Influence of sodium chloride and glucose on acid-induced gelation of heat-denatured ovalbumin

ABSTRACT:  We examined the effects of NaCl and glucose on cold-set ovalbumin gelation. Cold-set gels were prepared by adding glucono-δ-lactone (GDL) to a 2% heated ovalbumin solution. For the gel prepared from ovalbumin heat-denatured with NaCl and glucose, the gel with 10 mM NaCl was most transparent and had high gel strength. Its maximum complex shear modulus ( G *) and turbidity were 2.5 times greater and 3 times lower, respectively, than those of the gel without NaCl. The turbidity of the gel with the higher NaCl content increased steeply after the addition of GDL and did not change during the experimental period. The maximum G * of the gel exhibited positive correlations with the molar mass, radius, and surface hydrophobicity of soluble aggregates and the NaCl content, but the turbidity exhibited negative correlations with these factors. The presence of glucose did not significantly affect the turbidity or rheological properties of the gel. For the gel prepared by adding NaCl and glucose with GDL, the presence of glucose did not affect the turbidity, but the maximum G * decreased in inverse proportion to the glucose content. The turbidity of the gel with higher NaCl content (≥ 50 mM) was the greatest among all samples, and the increased turbidity was maintained throughout the measurements. The gels with 50 and 100 mM NaCl exhibited thixotropy during shearing at a constant shear rate. Therefore, the presence of NaCl and glucose during cold gelation could facilitate the preparation of cold-set gels having various properties for food applications.     

Protein Denaturation,Rheology, and Gelation Characteristics of Radio-Frequency Heated Egg White Dispersions

Gel properties of radio frequency (RF) heated egg white dispersions at 27.12 MHz were studied as function of concentration (2.5–2.5 kg/100 kg sample), pH (3–11) and heating time (60–180 s). Egg white dispersions demonstrated a gradual liquid-solid transformation as they denatured and gelled during RF treatment. The critical concentration and heating period for egg white protein denaturation and gelation were found to be 7.5% (w/w) and 150 seconds. The elastic modulus (G′) of RF-heated samples increased with concentration and heating period (temperature), whereas complex viscosity (η*) increased exponentially with concentration. In an alkaline condition, the egg white dispersion did not produce a gel; however, in acidic condition it resulted in a strong gel with significantly (P?<?0.05) higher G′. This could be attributed to the high dielectric constant (ε′) and loss factor (ε″) values of acidified samples as compared to the alkaline and control egg white dispersion. Effect of heating rate (1, 5, 10, and 20°C/min) in situ on rheometer plate significantly affected gel rigidity; the RF treated sample rigidity was comparable to samples heated at the rate of 5 and 10°C/min. Differential scanning calorimetry, dielectric measurement, and sodium dodecyl sulfate (SDS) PAGE electrophoresis results were used to confirm gelation behavior during both conventional and RF heating conditions.     

Effect of heating temperature and sodium chloride concentration on ultrastructure and texture of gels made from giant squid (Dosidicus gigas) with addition of starch,l-carrageenan and egg white

This paper seeks to compare the ultrastructure of gels made from frozen muscle of giant squid (Dosidicus gigas) at various temperatures with a number of different rheological parameters, with reference to a variety of added ingredients (non-muscle proteins and hydrocolloids) and to NaCl concentration. Interesting data on gel rheological properties were found where formulae containedl-carrageenan, starch and egg white, with a low salt concentration (1.5%). This seems to be because carrageenan forms an independent network which supports the principal structure formed by the fish protein; starch is incorporated into the network and retains water; and egg white forms a supplementary network which helps to improve rheological properties.     

Effect of heating temperature and sodium chloride concentration on ultrastructure and texture of gels made from giant squid (Dosidicus gigas) with addition of starch,l-carrageenan and egg white

This paper seeks to compare the ultrastructure of gels made from frozen muscle of giant squid (Dosidicus gigas) at various temperatures with a number of different rheological parameters, with reference to a variety of added ingredients (non-muscle proteins and hydrocolloids) and to NaCl concentration. Interesting data on gel rheological properties were found where formulae containedl-carrageenan, starch and egg white, with a low salt concentration (1.5%). This seems to be because carrageenan forms an independent network which supports the principal structure formed by the fish protein; starch is incorporated into the network and retains water; and egg white forms a supplementary network which helps to improve rheological properties.     

Texture Profile Analysis, Expressed Serum, and Microstructure of Heat-Formed Egg Yolk Gels

Egg yolk gels were formed by heating previously stirred egg yolk, having various pHs, protein concentrations, and NaCl levels, at various times and temperatures. Texture profiles were obtained by an Instron double-compression test, and serum was expressed from frozen-thawed gels. Microstructures of selected gels were observed by scanning electron microscopy. Gel hardness generally increased with increasing pH, protein or salt concentration, temperature, and length of heating time. The amount of serum expressed from gels decreased as gel hardness increased. Cohesiveness and springiness of gels increased with time and temperature. Gel microstructure consisted of spheres (4–50 μm) and granules (0.3–1.0 μm) dispersed in a continuous matrix. Spheres were physically disrupted by dilution and by addition of salt.     

Influence of pH and Salts on Egg White Gelation

ABSTRACT: Egg white is used in food products for various functional properties. These are strongly influenced by pH, ionic strength, type and concentration of salts. Through an experimental design strategy, the aim of this study was to quantify the influence of pH, cations, and anions naturally present in egg white, and of citrate on egg white gelation. Results showed that pH and Fe³⁺ modified the coagulation temperature of egg white and consequently, the gel characteristics. High concentrations of NaCl decreased the water-holding capacity and the microstructure of egg white gels. At pH 7, viscoelastic properties and microstructure of egg white gels were altered by Ca²⁺ and Mg²⁺ addition.     

Simple and Rapid Method for Measuring Turbidity in Gels and Sols from Milk Whey Protein

Protein isolates prepared from acid whey concentrate and cheese whey concentrate, and β-lactoglobulin were studied. Turbidity of samples was measured using a 96-well microplate and a microreader. This method allowed many (>100) small samples (< 250 μL) to be treated at the same time. At low ionic strength and at neutral to alkaline pH, samples were transparent after heating. Transparent gels could also be prepared in this region with a small amount of NaCl.